Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
UbiB kinase-like proteins exist in archaea, bacteria and eukaryotes, and comprise ~25% of all microbial protein kinase-like (PKL) enzymes. The founding member of the UbiB family, UbiB from Escherichia coli, supports the biosynthesis of ubiquinone, also known as coenzyme Q (CoQ), by an unknown mechanism. In eukaryotes, UbiB homologues are found exclusively in mitochondria, where they likewise have been connected to CoQ biosynthesis (for a review, see Trends Biochem. Sci.42, 824–843; 2017).
Enjoying our latest content?
Log in or create an account to continue
Access the most recent journalism from Nature's award-winning team
Explore the latest features & opinion covering groundbreaking research
This article is part of a series from the NIH Common Fund Illuminating the Druggable Genome (IDG) programme. The goal of IDG is to catalyse research on understudied proteins from druggable gene families by providing reagents, phenotypes and a mineable database, focusing on G protein-coupled receptors, kinases and ion channels. For more information, see https://druggablegenome.net/. Work was also supported by NIH R35GM131795 (D.J.P.) and NIH T32GM008505/NSF DGE-1747503 (N.H.M.).
